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FAQ: Troubleshooters - Info Required When Posting - Read This First - Do NOT Ignore ! Information required when posting (ignore this at the risk of being ignored)2. FAQ: Common Issues (Read This First before posting)3. Clean Install instructions. SB Live/Audigy issue with gen_nomad. Problems caused by using 3rd- party MP3. Pro plugin. 6. Problems with Internet TV/Radio Streams or Video playback?. DRM- Protected WMA playback issues? Read This First)7. Tips and Tricks for MSVCRT. Errors. 8. Not happy with 5. Online Services / Shoutcast browser? Read this first! 9. Most Requested Features / Plug- ins. Winamp 5. x Component List (full list/details of Winamp installation options)~ Updated by Nunzio. Apr 2. 00. 5 | above links no longer open separate windows ~__________________________________________________________________________SB Live/Audigy Sound Card Users, READ THISBefore you ask for help make sure you delete gen_nomad. This faulty plug- in silently installed by Creative Play. Center has been known to cause serious problems with Winamp. For more information please refer to this thread. You can also delete Ctn. Plugin. Res. crl which is associated/installed with gen_nomad. Other Information: Tech Support Greatest Hits > Offical 3rd- party Plugin Buglist > gen_nomad. From Tech Support Greatest Hits > Useful Links to Common Problems & Questions Previously Asked: SBLive & Play. Center. 2 related issues: http: //forums. Latest drivers: 1 | 2 | 3. RE: How do I remove 3rd- party plug- inshttp: //forums. For all SB Audigy specific issues: http: //forums. Live! and Audigy cards in this thread)Sign this petition to demand better tech support / drivers from Creative: http: //www. Skipping with Direct. Soundhttp: //forums. Start > Run > dxdiag > OK > Sound Tab: Reduce the "Direct. Sound Acceleration" slider (to Basic)Note that none of the above issues exist with newer Creative cards, eg. X- Fi : -)~ Updated by DJ- Egg : 1. July 2. 00. 2 | 2. May 2. 00. 3 ~~ Updated by Sawg : 2. April 2. 00. 2 ~_________________________________________________________________________Problems caused by using 3rd- party MP3. Pro plugin. THOMSON mp. PRO Decoder Plug- in for Winamp. The buggy 3rd- party MP3. Pro plugin (in_mp. Thomson/mp. 3prozone is known to cause the following problems: -Does not parse metadata to the media library; therefore artist, album, track#, title info is not read/displayed when importing mp. Does not support Shoutcast streaming titles (displays the station name/url only).- Does not read/support ID3v. Lyrics. 3 tags (reads ID3v. Does not support Advanced Title Formatting- Does not support any unicode/international characters in filenames/tags.- Does not work properly with Winamp's built- in CD Ripping/Burning engine.- Does not correctly read some xing/vbr headers, causing tracktimes to display as 0: 0. Does not support seeking in some vbr- encoded mp. Breaks aac. 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Why not to use WMA/mp. Basically, MP3. Pro is now widely known to be a dead format. It has already been replaced by the newer aac. Plus technology, which is already supported by in_mp. Winamp 5. x distro. Native MP3. Pro support will NEVER be implemented in Winamp, mainly due to licensing issues/costs and the fact that it is a truly lousy and dead format. More info about AACPlushttp: //www. Plus. htmhttp: //www. Updated by DJ Egg : 7th Jan 2. Compiled, maintained and updated for Winamp 5. DJ Egg. Clean Install Instructions. Note: You only need to do a clean install if you are experiencing problems that cannot be resolved using any other method. If you are just upgrading to a newer version of Winamp 5. Winamp 2. x or 5. Winamp. 3), thus keeping all your current settings etc. Important: If the problems persist after carrying out all the instructions below,please read this section before posting on the forums. Quick Uninstall - > Reinstall: Note, you will lose all settings, bookmarks, skins, library database/playlists, etc by choosing this method. If you need to backup anything first, then please use the 2nd method below instead. Uninstall Winamp (via Control Panel > Add/Remove Programs)2. Delete the Winamp dir (where Winamp was installed)3. Delete the contents of the %App. Data%\Winamp folder (see below for more info). Delete C: \Windows\Winamp. Reinstall Winamp. Full Uninstall - > Reinstall procedure: Winamp 5. Backup. Note: You don't need to backup anything if you don't want to, ie. Auto Backup: As from Feb 2. Winamp Backup Tool to backup everything (settings, playlists, bookmarks, database, skins, etc)Manual Backup: i) If you haven't done so already, save your playlist to . Unicode . m. 3u. 8) via: Playlist - > List button - > Save(mainly applicable to people who use one single large playlist all the time). And do NOT save it to the Winamp folder. Close Winampiii) Navigate to the Winamp settings folder via 'My Computer'Usually %App. Data%\Winamp (for multi- user setups / more info)Or: C: \Program Files\Winamp (for old 'shared' setups on upgrades)Here is the list of files that some people might want to backup: * The bookmark list = winamp. Any saved EQ presets = winamp. Q1 winamp. Q2 & . EQF files* The remote cddb database = Plugins\Gracenote\cddb. The local cddb database = Plugins\cddiscs. Plugins\in_cdda. cdb | 5. The Playlist Generator database: Plugins\Gracenote\cddbplm. The skins in the Skins dir (. Don't backup the Plugins dir, not unless you know for sure there's one or more rare / hard to find plugins or avs presets in there. In which case, just backup the plugins & presets of your choice, not the whole folder. Naturally, you should still have copies of the setup files for any 3rd- party plugins you've downloaded, so you can always use these to reinstall 3rd- party plugins later. Winamp 2. 9x and 5. Library data by using the uninstall procedure outlined below. You can also backup: * The ML config file, gen_ml. Winamp\Plugins dir) * The "Winamp\Plugins\ml" dir(main Local Media database files = main. ML Playlists = playlists. History = recent. Note: Winamp 5. 5. Database Import/Export" plugin (ml_impex. Media Library - > Library button - > Import/Export Database). Tips on backing up ratings can be found here* Note: If you selected "separate settings per user" in the 5. App. Data%\Winamp folder instead.%App. Data% is a hidden folder by default, so you may need to make sure you can view hidden files & folders first via: Control Panel - > Folder Options - > View tab. App. Data%\Winamp is usually found at "C: \Documents and Settings\(username)\Application Data\Winamp" (Win. XP), or "C: \Users\(username)\App. Data\Roaming\Winamp" (Vista), though you can just type %App. Data%\Winamp into the Windows address bar (or via: Start - > Run) and hit Enter. In Winamp 5. 5 and higher, settings are automatically saved in %App. Data%\Winampexcept for on upgrades from previous versions, where 'shared' setups are still respected. It is strongly recommended to start fresh with clean settings. You can always change settings back to taste after Winamp 5 is up and running. But, if you really need to backup any config files, full details can be found here. Uninstalli) Check to see if you've installed any other 3rd party plugins that also may have created entries in Add/Remove Programs (eg. Album. List, Sqr. Sft, Powerplayer, etc). If so, uninstall these before Winamp*Note: In Winamp 5. Get the Most out of Winamp' page in the Installer Options: Winamp Remote (Orb Networks), Winamp Toolbar (AOL), Emusic Icon & Offer. Liquid chromatography–mass spectrometry - Wikipedia. Liquid chromatography–mass spectrometry (LC- MS) is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography (or HPLC) with the mass analysis capabilities of mass spectrometry (MS). Coupled chromatography - MS systems are popular in chemical analysis because the individual capabilities of each technique are enhanced synergistically. While liquid chromatography separates mixtures with multiple components, mass spectrometry provides structural identity of the individual components with high molecular specificity and detection sensitivity. This tandem technique can be used to analyze biochemical, organic, and inorganic compounds commonly found in complex samples of environmental and biological origin. Therefore, LC- MS may be applied in a wide range of sectors including biotechnology, environment monitoring, food processing, and pharmaceutical, agrochemical, and cosmetic industries.[1][2]In addition to the liquid chromatography and mass spectrometry devices, an LC- MS system contains an interface that efficiently transfers the separated components from the LC column into the MS ion source.[2][3] The interface is necessary because the LC and MS devices are fundamentally incompatible. While the mobile phase in a LC system is a pressurized liquid, the MS analyzers commonly operate under vacuum (around 1. Thus, it is not possible to directly pump the eluate from the LC column into the MS source. Overall, the interface is a mechanically simple part of the LC- MS system that transfers the maximum amount of analyte, removes a significant portion of the mobile phase used in LC and preserves the chemical identity of the chromatography products (chemically inert). As a requirement, the interface should not interfere with the ionizing efficiency and vacuum conditions of the MS system.[2] Nowadays, most extensively applied LC- MS interfaces are based on atmospheric pressure ionization (API) strategies like electrospray ionization (ESI), atmospheric pressure chemical ionization (APCI), and atmospheric pressure photo- ionization (APPI). These interfaces became available in the 1. History of LC- MS[edit]The coupling of chromatography with MS is a well developed chemical analysis strategy dating back from the 1. Gas chromatography (GC) - MS was originally introduced in 1. A. T. James and A. J. P Martin were trying to develop tandem separation - mass analysis techniques.[5] In GC, the analytes are eluted from the separation column as a gas and the connection with electron ionization (EI) or chemical ionization (CI) ion sources in the MS system was a technically simpler challenge. Because of this, the development of GC- MS systems was faster than LC- MS and such systems were first commercialized in the 1. The development of LC- MS systems took longer than GC- MS and was directly related to the development of proper interfaces. V. L. Tal'roze and collaborators started the development of LC- MS in the early 1. LC columns and MS ion sources.[6][4] A similar strategy was investigated by Mc. Lafferty and collaborators in 1. This was the first and most obvious way of coupling LC with MS, and was known as the capillary inlet interface. This pioneer interface for LC- MS had the same analysis capabilities of GC- MS and was limited to rather volatile analytes and non- polar compounds with low molecular mass (below 4. Da). In the capillary inlet interface, the evaporation of the mobile phase inside the capillary was one of the main issues. Within the first years of development of LC- MS, on- line and off- line alternatives were proposed as coupling alternatives. Liquid chromatography–mass spectrometry (LC-MS) is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography (or. · An UPLC-ESI-MS/MS Assay Using 6-Aminoquinolyl-N-Hydroxysuccinimidyl Carbamate Derivatization for Targeted Amino Acid Analysis: Application to Screening of. Request the new 2013 Essential Chromatography and Spectroscopy Catalog or download each chapter individually. Grow your lab with the very best products and applications. · A Validated Stability-indicating Reverse Phase HPLC Assay Method for the Determination of Memantine Hydrochloride Drug Substance with UV-Detection Using. In general, off- line coupling involved fraction collection, evaporation of solvent, and transfer of analytes to the MS using probes. Off- line analyte treatment process was time consuming and there was an inherent risk of sample contamination. Rapidly, it was realized that the analysis of complex mixtures would require the development of a fully automated on- line coupling solution in LC- MS.[4]Moving- belt interface[edit]The moving- belt interface (MBI) was developed in 1. This interface consisted of an endless moving belt receiving the LC column effluent. On the belt, the solvent was evaporated by gently heating and efficiently exhausting the solvent vapors under reduced pressure in two vacuum chambers. After removing the liquid phase, the analytes would desorb from the belt and migrate to the MS ion source to be analysed. MBI was successfully used for LC- MS applications between 1. LC to MS devices using EI, CI, and fast- atom bombardment (FAB) ion sources. The most common MS systems connected by MBI interfaces to LC columns were magnetic sector and quadropole instruments. MBI interfaces for LC- MS allowed MS to be widely applied in the analysis of drugs, pesticides, steroids, alkaloids, and polycyclic aromatic hydrocarbons. This interface is no longer used because of its mechanical complexity and the difficulties associated to belt renewal. Particle beam interfaces took over the wide applications of MBI for LC- MS in 1. Direct liquid introduction interface[edit]The direct liquid introduction (DLI) interface was developed in 1. This interface was thought as a solution to the evaporation of liquid inside the capillary inlet interface. In DLI, a nebulizer was used to disintegrate part of the effluent coming from the column. A small diaphragm was used to form a liquid jet composed of small droplets that were subsequently dried in a desolvation chamber. A microbore capillary column was used to transfer the nebulized liquid product to the MS ion source. The analytes were ionized using a solvent assisted chemical ionization source, where the LC solvents acted as reagent gases. To use this interface, it was necessary to split the flow coming out of the LC column because only a small portion of the effluent (1. MS vacuum. One of the main operational problems of the DLI interface was the frequent clogging of the diaphragm orifices. The DLI interface was used between 1. B1. 2. However, this interface was replaced by the thermospray interface, which removed the flow rate limitations and the issues with the clogging diaphragms.[2][4]Thermospray interface[edit]The thermospray (TSP) interface was developed in 1. Vestal laboratories at the University of Houston. The interface resulted from a long term research project intended to find a LC- MS interface capable of handling high flow rates (1 ml/min) and avoiding the flow split in DLI interfaces. The TSP interface was composed by a heated probe, a desolvation chamber, and an ion exchange skimmer. The LC effluent passed through the heated probe and emerged as a jet of vapor and small droplets flowing into the desolvation chamber at low pressure. The ionization of solutes occurred by direct evaporation or ion- molecule reactions induced by the solvent. This interface was able to handle up to 2 ml/min of eluate from the LC column and would efficiently introduce it into the MS vacuum system. TSP was also more suitable for LC- MS applications involving reversed phase liquid chromatography (RT- LC). The TSP system had a dual function acting as an interface and a solvent- mediated chemical ionization source. With time, the mechanical complexity of TSP was simplified, and this interface became popular as the first ideal LC- MS interface for pharmaceutical applications comprising the analysis of drugs, metabolites, conjugates, nucleosides, peptides, natural products, and pesticides. The introduction of TSP marked a significant improvement for LC- MS systems and was the most widely applied interface until the beginning of the 1. API).[2][3][7]FAB Based Interfaces[edit]The frit FAB and continuous flow- FAB (CF- FAB) interfaces were developed in 1. Both interfaces were similar, but they differed in that the first used a porous frit probe as connecting channel, while CF- FAB used a probe tip. From these, the CF- FAB was more successful as a LC- MS interface and was useful to analyze non- volatile and thermally labile compounds. In these interfaces, the LC effluent passed through the frit or CF- FAB channels to form an uniform liquid film at the tip. There, the liquid was bombarded with ion beams or high energy atoms (fast atom). For stable operation, the FAB based interfaces were able to handle liquid flow rates of only 1- 1. In order to be used in FAB MS ionization sources, the analytes of interest should be mixed with a matrix (e. Application to Screening of Arabidopsis thaliana Mutants. Abstract. In spite of the large arsenal of methodologies developed for amino acid assessment in complex matrices, their implementation in metabolomics studies involving wide- ranging mutant screening is hampered by their lack of high- throughput, sensitivity, reproducibility, and/or wide dynamic range. In response to the challenge of developing amino acid analysis methods that satisfy the criteria required for metabolomic studies, improved reverse- phase high- performance liquid chromatography- mass spectrometry (RPHPLC- MS) methods have been recently reported for large- scale screening of metabolic phenotypes. However, these methods focus on the direct analysis of underivatized amino acids and, therefore, problems associated with insufficient retention and resolution are observed due to the hydrophilic nature of amino acids. It is well known that derivatization methods render amino acids more amenable for reverse phase chromatographic analysis by introducing highly- hydrophobic tags in their carboxylic acid or amino functional group. Therefore, an analytical platform that combines the 6- aminoquinolyl- N- hydroxysuccinimidyl carbamate (AQC) pre- column derivatization method with ultra performance liquid chromatography- electrospray ionization- tandem mass spectrometry (UPLC- ESI- MS/MS) is presented in this article. For numerous reasons typical amino acid derivatization methods would be inadequate for large scale metabolic projects. However, AQC derivatization is a simple, rapid and reproducible way of obtaining stable amino acid adducts amenable for UPLC- ESI- MS/MS and the applicability of the method for high- throughput metabolomic analysis in Arabidopsis thaliana is demonstrated in this study. Overall, the major advantages offered by this amino acid analysis method include high- throughput, enhanced sensitivity and selectivity; characteristics that showcase its utility for the rapid screening of the preselected plant metabolites without compromising the quality of the metabolic data. The presented method enabled thirty- eight metabolites (proteinogenic amino acids and related compounds) to be analyzed within 1. M (i. e., atomole level on column), which represents an improved sensitivity of 1 to 5 orders of magnitude compared to existing methods. Our UPLC- ESI- MS/MS method is one of the seven analytical platforms used by the Arabidopsis Metabolomics Consortium. The amino acid dataset obtained by analysis of Arabidopsis T- DNA mutant stocks with our platform is captured and open to the public in the web portal Plant. Metabolomics. org. The analytical platform herein described could find important applications in other studies where the rapid, high- throughput and sensitive assessment of low abundance amino acids in complex biosamples is necessary. Keywords: 6- aminoquinolyl- N- hydroxysuccinimidyl carbamate, amino acid analysis, UPLC- ESI- MS/MS, metabolomics, Arabidopsis thaliana, mutant screening. Introduction. In the post genomics era where the plant biology community is facing the challenge of identifying the functionalities of genes of unknown function (GUFs), metabolomics offers a link between biochemical phenotype and gene function [1]. However, the use of metabolomics for the prediction of the function of plant genes faces technical challenges due to the large size (between 1. These challenges are currently being tackled by combining targeted and non- targeted metabolic analyses to characterize and compare changes in metabolic networks [1,2,5,6,7]. Those combined strategies are a partial solution to the lack of universality of a single analytical technique, as they exploit the power of current separation technologies and the various dynamic ranges and sensitivities offered by the arsenal of commercially available analytical detectors to cover a larger portion of the metabolome than any single platform alone [2,5,6,7,8]. Currently, combined metabolomics technologies are being tested as functional genomic tools for the annotation of Arabidopsis thaliana GUFs [1,7,9]. Usually, high throughput biochemical screening methods are employed to first identify previously uncharacterized Arabidopsis mutants affecting a variety of metabolic pathways. The screening is carried out by targeted analysis of specific groups of compounds or metabolic subsets (glucosinolates, fatty acids, phytosterols, isoprenoids, amino acids, among others) across a large population of mutagenized Arabidopsis lines. Once new loci involved in plant metabolism are identified further work is performed in those particular mutants using non- targeted analysis in order to characterize metabolite changes more broadly. Identification of metabolites that are discriminatory between the knockout plant compared to the wild- type help fill up the gaps in our understanding of plant- specific regulatory and biosynthetic pathways and determine the function of the GUFs [1,7,9]. Because of the central role that amino acids play in plant biochemistry, screening methods that quantify free levels of this class of metabolites in plant tissue are in demand. Despite the numerous methods available for amino acid analysis, many lack the suitability for metabolomic studies. Three aspects are vital in developing an effective targeted metabolite analysis platform for large- scale mutant screening: (i) reduction of sample preparation and analysis time, (ii) collection of high- quality data, and (iii) broad dynamic range [1. Chromatographic separation methods (gas chromatography, GC, and liquid chromatography, LC) combined with tandem mass spectrometric (MS/MS) detection are dominating the field of metabolomics. Although considerable work has been done in the development of LC- MS methods for analysis of both underivatized and derivatized amino acids in complex matrices, the former are being particularly implemented in metabolomic research and employ the ion- pairing (IP) reversed- phase (RP) LC [1. HILIC) alternatives [1. Although these methodologies are very attractive due to the elimination of the sample derivatization step, they suffer of several problems. In IPRPLC, for example, the occurrence of system peaks during the gradient elution disturbs the quantitation of amino acids. Systems peaks are caused by low volatility of ion- pairing reagents (example, pentadecafluorooctanoic acid, PDFOA) and their adsorption on the column support surface [1. In addition, long equilibration times (te) between runs and column regeneration after few injections are needed in order to avoid degradation in chromatography and retention time drift for amino acids due to accumulation of the ion- pairing reagent on the column surface. Equilibration times from 9 to 1. Another drawback associated with the use of ion- pairing reagents in LC- ESI- MS analysis is the decrease in ionization efficiency of amino acids due to interference by these easy- ionized mobile phase modifiers [2. The occurrence of undesirable reactions between ion- pairing reagents and salts present in biological samples can also contribute to this problem. Armstrong et al. [2. TDFHA) during the analysis of 2. IPRPLC coupled to time- of- flight (TOF) MS which caused significant signal suppression of alanyl- glutamine dipeptide and valine. A cation- exchange cleanup step had to be added to the sample preparation in order to decrease the abundance of the TDFHA adduct and improve the accuracy and precision of the analysis [2. Last but not least, surfactant impurities can make the eluent particularly noisy at the m/z range corresponding to underivatized amino acids, affecting the sensitivity of the analysis [1. Alternatively, when HILIC separation mode is used instead of a reversed- phase system underivatized amino acids are retained without any mobile phase modifier and the above mentioned drawbacks associated to the use of iron- pairing reagents can be avoided. Despite of that, column care (i. HILIC analysis. Furthermore, HILIC columns suffer of poor separation efficiency compared to the RPLC technique [2. Due to the above, it is necessary to explore the possibility of implementing LC- MS methods for the analysis of derivatized amino acids to large- scale mutant screening in metabolomic studies. 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